The primary objective of this proposal is to obtain a 500 MHz nuclear magnetic resonance spectrometer for five research groups within the Departments of Chemistry and Biochemistry at Texas A&M University. The instrument shall be utilized to solve structural and mechanistic problems involving PHS supported biomedical research. The Scott laboratory is addressing the structural intermediates in the biosynthesis of chlorophyll, vitamin-B12, penicillin and related molecules. The Pace laboratory is pursuing structural intermediates in protein folding using ribonuclease T1 as a model system. Reaction intermediates and dynamics of the reaction catalyzed by carbamoyl phosphate synthetase, phosphotriesterase, and bacterial luciferase are being probed by the Raushel laboratory. The Barton group is using high field NMR spectroscopy to determine the complex structures constructed in their organic synthesis program. The structures of novel amino acid and peptide mimics from controlled radical reactions are being investigated by the Newcomb laboratory.